ID   NADK_CYTH3              Reviewed;         292 AA.
AC   Q11PL9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
DE            EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE   AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361};
GN   OrderedLocusNames=CHU_3408;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC   Cytophagaceae; Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / JCM 20678 / CIP 103989 / IAM 12607 /
RC   NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC       NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC       Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC       adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + ATP = ADP + NADP(+) + H(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
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DR   EMBL; CP000383; ABG60644.1; -; Genomic_DNA.
DR   RefSeq; WP_011586751.1; NC_008255.1.
DR   AlphaFoldDB; Q11PL9; -.
DR   SMR; Q11PL9; -.
DR   STRING; 269798.CHU_3408; -.
DR   KEGG; chu:CHU_3408; -.
DR   eggNOG; COG0061; Bacteria.
DR   HOGENOM; CLU_008831_0_3_10; -.
DR   OMA; AADFEFT; -.
DR   OrthoDB; 9774737at2; -.
DR   Proteomes; UP000001822; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019674; P:NAD+ metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP+ biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 1.
DR   HAMAP; MF_00361; NAD_kinase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR064509; NAD_kinase_N.
DR   InterPro; IPR002504; NADK.
DR   NCBIfam; NF002521; PRK01911.1; 1.
DR   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF0; NAD KINASE; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..292
FT                   /note="NAD kinase"
FT                   /id="PRO_1000059866"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         74..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         147..148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         188..193
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   292 AA;  32909 MW;  1FF5C7A3054FFD40 CRC64;
     MIFALHGRPF KEDNIPYVQH LLYYLQKKEI QFLINESFVD YLVQCNILLP SFFTTFTNKT
     DLGKPDLMLS IGGDGTLLES ATFIGDQNIP LVGINTGRLG FLATTPREEL EGSVDELISG
     SYKLSERTLI KLISDEKLFG DLNFAMNEFA LTKRDSSSMI TVHTYIDGEF LNSYWADGLL
     VSTPTGSTGY SLSCGGPLVH PKTENFIITP ISPHNLNVRP MIVPDSCHIS FEIEGRNQNF
     LISLDSRAEI VSSNIKLSVK KEDFKIQLVE LKNYNYYKTL RSKLNWGLDA RN
//